Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.6.1 (sulfatase)
 3,205 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Arylsulfatase (EC 3.1.6.1) activity in human stromal cells isolated from specimens of histologically normal proliferative endometrium was increased several-fold during culture for 8-15 days in RPMI-1640 medium plus 10% charcoal-treated fetal bovine serum in the presence of a mixture of ovarian hormones (36 nM estradiol, 1 microM medroxyprogesterone acetate, and 100 micrograms/mL relaxin). The changes in sulfatase activity, determined by measuring the rate of formation of estrone from tritiated estrone sulfate, were associated with in vitro decidualization of the stromal cells, as determined by changes in secretion of PRL into daily renewed culture medium. PRL output by the cells during the last 24 h in culture and sulfatase activity in the cells collected at the end of the culture period were related to their DNA and protein contents. Sulfatase activity in the cells cultured in the presence of the ovarian hormones was comparable to the activity found in decidual cells at term pregnancy. PRL added for 1 day to cultures of stromal cells in the absence of exogenous hormones increased sulfatase activity in the cells, probably by acting in an autocrine manner, as previously demonstrated with human decidual cells during pregnancy. These experiments also revealed a hormonal regulation of stromal cell proliferation in vitro, as estimated from measurements of both DNA and protein levels per dish. Augmentation of sulfatase activity can serve as another marker of in vitro decidualization. Physiologically, an increase in this enzymatic activity may result in a preferential estrogenic stimulation of the decidualized cells by utilization of a circulating substrate, estrone sulfate. This hypothesis could explain the preferential retention of progesterone receptors in decidual cells observed immunohistochemically during the late luteal phase of the menstrual cycle, suggestive of a shift in progestogenic actions from the epithelium to the stroma.
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PMID:Estrone sulfate sulfatase activity is increased during in vitro decidualization of stromal cells from human endometrium. 229 51

Homogeneous preparations of decidual cells were obtained from term decidual tissue adherent to fetal membranes by using a slightly modified version of a technique developed for the isolation of decidual cells from first and second trimester decidua. The effects of human PRL (hPRL) and oxytocin on the kinetics of the hydrolysis of estrone sulfate were determined in decidual cells prepared from tissue obtained before and after the onset of labor. In addition, sulfatase activity in decidual cells isolated from term decidua was compared with those of chorionic cells isolated from chorion leave of the same pregnancy. Chorionic cells had significantly higher (mean, 2.5-fold) levels of sulfatase activity than the corresponding decidual cells. The mean sulfatase activity in decidual cells obtained after normal vaginal delivery [25 +/- 19 (+/- SE) nmol/mg protein X 15 min) was higher than that in decidual cells obtained from patients undergoing cesarean section before the onset of labor (1.7 +/- 0.11). This difference was significant (P less than 0.02, by Mann-Whitney test) in spite of the large variation in activity in preparations from vaginal deliveries. hPRL (500 ng/ml) and oxytocin (0.2 microM) had similar effects on sulfatase activity in decidual cells in a manner dependent on whether the cells were isolated from tissue obtained before or after labor. In cells isolated from fetal membranes obtained before labor (cesarean delivery), hPRL or oxytocin significantly stimulated sulfatase activity, whereas in decidual cells obtained after vaginal delivery, both hPRL and oxytocin significantly inhibited sulfatase activity. The Michaelis constants for the hydrolysis of estrone sulfate (Km, 22 +/- 4.8 microM) were not affected by these hormones. Since the mean sulfatase activity of decidual cells obtained before labor was approximately 10-fold higher than the activity reported for endometrial stromal cells, PRL produced by decidual cells may act in vivo as an autocrine factor to stimulate their sulfatase activity.
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PMID:In vitro effects of human prolactin and oxytocin on sulfatase activity in isolated human decidual cells. 373 40